β-structure of the coat protein subunits in spherical particles generated by tobacco mosaic virus thermal denaturation
β-structure of the coat protein subunits in spherical particles generated by tobacco mosaic virus thermal denaturation
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DOI：
10.1080/07391102.2013.788983
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发表时间：
2014-05-04
影响因子：
4.4
通讯作者：
Atabekov, Joseph G.
中科院分区：
文献类型：
--
作者：
Dobrov, Evgeny N.;Nikitin, Nikolai A.;Atabekov, Joseph G.
1956年，R.G.哈特（R.G. Hart）描述了棒状烟草花叶病毒（TMV）病毒粒子在90-98℃的热变性下转化为“球状颗粒”的过程。我们最近报道了由TMV在94-98℃热变性产生的球形颗粒（SPs）具有高度稳定、不含rna和不溶于水的特性。SPs形状一致，但大小差异很大（53 ~ 800 nm），这取决于病毒浓度。在这里，我们用圆二色性、荧光光谱和拉曼光谱描述了SPs的一些结构特征。研究发现，SPs蛋白的结构与天然TMV有很大的不同，其特征是外壳蛋白亚基从主要（约50%）的α -螺旋结构转变为α -螺旋含量低、β -片含量高的结构。SPs与硫黄素T有强烈反应，提示形成淀粉样结构。
Conversion of the rod-like tobacco mosaic virus (TMV) virions into "ball-like particles" by thermal denaturation at 90-98 degrees C had been described by R.G. Hart in 1956. We have reported recently that spherical particles (SPs) generated by thermal denaturation of TMV at 94-98 degrees C were highly stable, RNA-free, and water-insoluble. The SPs were uniform in shape but varied widely in size (53-800 nm), which depended on the virus concentration. Here, we describe some structural characteristics of SPs using circular dichroism, fluorescence spectroscopy, and Raman spectroscopy. It was found that the structure of SPs protein differs strongly from that of the native TMV and is characterized by coat protein subunits transition from mainly (about 50%) alpha-helical structure to a structure with low content of alpha-helices and a significant fraction of beta-sheets. The SPs demonstrate strong reaction with thioflavin T suggesting the formation of amyloid-like structures.